Protein Family Models for Protein (Select 2125488006) - Protein Family Models

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Items: 8

Select item 4135151.

This domain is found associated with the Pfam tRNA synthetase class II domain (Pfam:PF00587) and represents the N-terminal domain of seryl-tRNA synthetase. [1]. 8654381. The crystal structure of the ternary complex of T.thermophilus. seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate. analogue reveals a conformational switch in the active site.. Cusack S, Yaremchuk A, Tukalo M;. EMBO J 1996;15:2834-2842. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF014458.5
Method:: HMM

Select item 4116552.

aminoacyl--tRNA ligase-related protein

This HMM finds multiple types of aminoacyl--tRNA ligase, such as those for Thr, Pro, His, and Ser in Escherichia coli. Because equivalog-level HMMs exist to identify full-length members of the tRNA ligase families, any protein receiving annotation from this HMM is most likely to be either a partial sequence or a tRNA ligase-related protein involved in some process other than protein translation on the ribosome.

GO Terms:

Molecular Function:: nucleotide binding (GO:0000166)

Molecular Function:: aminoacyl-tRNA ligase activity (GO:0004812)

Molecular Function:: ATP binding (GO:0005524)

Biological Process:: tRNA aminoacylation for protein translation (GO:0006418)

Date:: 2024-08-14

Family Accession:: NF012796.5
Method:: HMM

Select item 3913883.

new record, indexing in progress

Family Accession:

Select item 3899604.

new record, indexing in progress

Family Accession:

Select item 3479665.

new record, indexing in progress

Family Accession:

Select item 3468626.

new record, indexing in progress

Family Accession:

Select item 2306837.

serine--tRNA ligase

serine--tRNA ligase catalyzes the attachment of serine to tRNA(Ser)

Date:: 2023-03-15

Family Accession:: 11480938
Method:: Sparcle

Select item 191638.

serine--tRNA ligase

This HMM represents the serine--tRNA ligase found in most organisms. It is a class II tRNA ligase. The seryl-tRNA synthetases of two model archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model.